ID   IF2_CAMJJ               Reviewed;         871 AA.
AC   A1VXL9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN   OrderedLocusNames=CJJ81176_0171;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the essential components for the initiation of protein
CC       synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC       and promotes its binding to the 30S ribosomal subunits. Also involved
CC       in the hydrolysis of GTP during the formation of the 70S ribosomal
CC       complex. {ECO:0000255|HAMAP-Rule:MF_00100}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00100}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00100}.
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DR   EMBL; CP000538; EAQ73271.1; -; Genomic_DNA.
DR   RefSeq; WP_002868936.1; NC_008787.1.
DR   AlphaFoldDB; A1VXL9; -.
DR   SMR; A1VXL9; -.
DR   STRING; 354242.CJJ81176_0171; -.
DR   EnsemblBacteria; EAQ73271; EAQ73271; CJJ81176_0171.
DR   KEGG; cjj:CJJ81176_0171; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_4_1_7; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000000646; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   Gene3D; 3.40.50.10050; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00100_B; IF_2_B; 1.
DR   InterPro; IPR044145; IF2_II.
DR   InterPro; IPR006847; IF2_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR000178; TF_IF2_bacterial-like.
DR   InterPro; IPR015760; TIF_IF2.
DR   InterPro; IPR023115; TIF_IF2_dom3.
DR   InterPro; IPR036925; TIF_IF2_dom3_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR43381; PTHR43381; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 2.
DR   SUPFAM; SSF50447; SSF50447; 2.
DR   SUPFAM; SSF52156; SSF52156; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00487; IF-2; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   PROSITE; PS01176; IF2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..871
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008223"
FT   DOMAIN          370..537
FT                   /note="tr-type G"
FT   REGION          60..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..386
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          404..408
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          425..428
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          479..482
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          515..517
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         379..386
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         425..429
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         479..482
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   871 AA;  96094 MW;  B7D34F465D11B604 CRC64;
     MAKIRIHEIA KELGYDSKEI IEKANELGLG IKTASNAVEP EIAAAIYEYI QTREIPEAFK
     KNIKTPTAKK PKKENIKEQE KLNESEKKEP KKEEKLKQEV KKEELKIEKE NAKEEEKQEI
     IDAHKPQSLA SATLAKRRGL VIVKKKKDEE EIQVKKEEVK NSNDISINNE ERLSLKTMFS
     NADESLKKKK KEKKSFVASK KESTEKMNFL DEHDFGDISL DDEDEVVLPD FSVKEQEKPQ
     NINKKQPNFI RQAVGNSAGF GLEGGIQRRS RKKPSKKIEK KEVEEVGSVA ISKEIRVYEF
     ADKIGKSTSE VISKLFMLGM MTTKNDFLDE DAIEILAAEF GIEINIINEA DEFDYVKDYE
     EETDEKDLVT RAPVITIMGH VDHGKTSLLD YIRKSRVASG EAGGITQHVG AYMVEKNGRK
     ITFIDTPGHE AFTAMRARGA SITDIVIIVV AADDGVKPQT KEAINHAKAA GVPIIIAINK
     MDKEAANPDM VKTQLAEMEI MPVEWGGSYE FVGVSAKTGM GIEDLLEIVL LQADILELKA
     NPKSFAKASI IESSVQKGRG AAATIIVQNG TLTVGSTVVA GEAYGKVRAM SDDQGKALKE
     IKPGECGVIV GLSEVADAGE ILIAVKTDKE AREYANKRHE YNRQKELSKS TKVSIDELGA
     KIKEGNLKAL PVILKADVQG SLEALKASLE KLRNDEIKVN IIHSGVGGIT QSDIELASAS
     ENSIVLGFNI RPTGEVKERS KDKGVEIKTY NVIYNLLDDV KALLGGMMSP IISEEQLGQA
     EIRQVINVPK IGQIAGCMVT EGVINRGAKI RLIRDGVVVY EGNVSSLKRF KDDAKEVAKG
     YECGVGIEGC DDMRVGDYIE SYKEVEEQAS L